PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 28797284-12 2017 Immunohistochemistry results demonstrated a downregulation of p-ERK, E2F1, and RRM2 in mice receiving gambogic acid treatment and combination treatment. gambogic acid 102-115 ribonucleotide reductase M2 Mus musculus 79-83 32763454-0 2020 Osalmid, a novel identified RRM2 inhibitor, enhances radiosensitivity of esophageal cancer. osalmide 0-7 ribonucleotide reductase M2 Mus musculus 28-32 32763454-3 2020 Previous studies have reported that Osalmid could act as an RRM2 inhibitor. osalmide 36-43 ribonucleotide reductase M2 Mus musculus 60-64 33023155-4 2020 In mouse cells, iron shortage decreased protein abundance for iron-binding nucleotide metabolism enzymes (prominently XDH and ferritin homolog RRM2). Iron 16-20 ribonucleotide reductase M2 Mus musculus 143-147 33023155-4 2020 In mouse cells, iron shortage decreased protein abundance for iron-binding nucleotide metabolism enzymes (prominently XDH and ferritin homolog RRM2). Iron 62-66 ribonucleotide reductase M2 Mus musculus 143-147 33577819-6 2021 Zn2+ binding sites were predicted in the TDP-43"s N-terminal domain, in the linker region between RRM1 and RRM2 domain, within RRM2 domain and at the junction of the RRM2 and C-terminal domain (CTD), but none in the 311-360 region of CTD. Zinc 0-4 ribonucleotide reductase M2 Mus musculus 107-111 33577819-6 2021 Zn2+ binding sites were predicted in the TDP-43"s N-terminal domain, in the linker region between RRM1 and RRM2 domain, within RRM2 domain and at the junction of the RRM2 and C-terminal domain (CTD), but none in the 311-360 region of CTD. Zinc 0-4 ribonucleotide reductase M2 Mus musculus 127-131 33577819-6 2021 Zn2+ binding sites were predicted in the TDP-43"s N-terminal domain, in the linker region between RRM1 and RRM2 domain, within RRM2 domain and at the junction of the RRM2 and C-terminal domain (CTD), but none in the 311-360 region of CTD. Zinc 0-4 ribonucleotide reductase M2 Mus musculus 127-131 33577819-7 2021 Furthermore, we found that Zn2+ promotes the in vitro thioflavin-T-positive aggregations of C-terminal fragments (CTFs) termed TDP-432C and TDP-432C-A315T that encompass the RRM2 and CTD domains. Zinc 27-31 ribonucleotide reductase M2 Mus musculus 174-178 31468165-9 2019 A higher MCS was associated with concurrent use of glucocorticoids and a higher baseline MCS (mR2 21.7%, cR2 25.1%). mcs 9-12 ribonucleotide reductase M2 Mus musculus 94-97 31468165-9 2019 A higher MCS was associated with concurrent use of glucocorticoids and a higher baseline MCS (mR2 21.7%, cR2 25.1%). mcs 89-92 ribonucleotide reductase M2 Mus musculus 94-97 22517893-6 2012 In the present study, we found for the first time that 5-azaC is a potent inhibitor of RRM2 in leukemia cell lines, in a mouse model, and in BM mononuclear cells from acute myeloid leukemia (AML) patients. Azacitidine 55-61 ribonucleotide reductase M2 Mus musculus 87-91 28507282-7 2017 Pharmacological inhibition of mTORC1 with rapamycin, mTOR kinase with AZD8055 or protein kinase B with MK2206 resulted in decrease of RRM1 and RRM2 in Rh30 cells both in vitro and in mouse tumor xenografts. (5-(2,4-bis((3S)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol 70-77 ribonucleotide reductase M2 Mus musculus 143-147 28507282-7 2017 Pharmacological inhibition of mTORC1 with rapamycin, mTOR kinase with AZD8055 or protein kinase B with MK2206 resulted in decrease of RRM1 and RRM2 in Rh30 cells both in vitro and in mouse tumor xenografts. MK 2206 103-109 ribonucleotide reductase M2 Mus musculus 143-147 28507282-10 2017 In addition, TP53 mutant cancer cells had elevation of RRM1 and RRM2, which was reduced by rapamycin. Sirolimus 91-100 ribonucleotide reductase M2 Mus musculus 64-68 22174045-11 2012 Downregulation of proteins, such as MAPK, matrin-3 and ribonucleotide reductase, subunit RRM2, which are implicated in cell proliferation, was also observed in TBTO-treated cells. bis(tri-n-butyltin)oxide 160-164 ribonucleotide reductase M2 Mus musculus 89-93 22403396-7 2012 Here we show that although both RRM1 and RRM2 expression are markedly induced in mouse uterine stromal cells undergoing decidualization, only RRM2 is regulated by progesterone, a key regulator of decidualization. Progesterone 163-175 ribonucleotide reductase M2 Mus musculus 142-146 22403396-12 2012 Therefore, RRM2 may be an important effector of progesterone signaling to induce cell proliferation and decidualization in mouse uterus. Progesterone 48-60 ribonucleotide reductase M2 Mus musculus 11-15 21275172-0 2010 [Effect of cinobufotalin on growth of xenograft of endometrial carcinoma cell line ishikawa in nude mouse and its impact on RRM2 expression]. cinobufotalin 11-24 ribonucleotide reductase M2 Mus musculus 124-128 21946215-4 2011 Truncations were tested mainly within a second RNA recognition motif (RRM2) of TDP-43; when the truncation site was more C-terminal in an RRM2 domain, a TDP-43 CTF basically became less soluble and more phosphorylated in differentiated Neuro2a cells. CHEMBL408967 160-163 ribonucleotide reductase M2 Mus musculus 70-74 21946215-4 2011 Truncations were tested mainly within a second RNA recognition motif (RRM2) of TDP-43; when the truncation site was more C-terminal in an RRM2 domain, a TDP-43 CTF basically became less soluble and more phosphorylated in differentiated Neuro2a cells. CHEMBL408967 160-163 ribonucleotide reductase M2 Mus musculus 138-142 21946215-5 2011 We also found that cleavage at the third beta-strand in RRM2 leads to the formation of SDS-resistant soluble oligomers. Sodium Dodecyl Sulfate 87-90 ribonucleotide reductase M2 Mus musculus 56-60 21275172-1 2010 OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2). cinobufotalin 51-64 ribonucleotide reductase M2 Mus musculus 189-224 21275172-1 2010 OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2). cinobufotalin 51-64 ribonucleotide reductase M2 Mus musculus 226-230 21275172-1 2010 OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2). cinobufotalin 66-69 ribonucleotide reductase M2 Mus musculus 189-224 21275172-1 2010 OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2). cinobufotalin 66-69 ribonucleotide reductase M2 Mus musculus 226-230 20731881-3 2010 The serum ALT elevation, with a peak at 24 h after Gal-N+LPS intoxication, was markedly augmented by means of the R1-mAb and R2-mAb. Galactosamine 51-56 ribonucleotide reductase M2 Mus musculus 125-131 20731881-6 2010 Our in-vitro study showed that R1-mAb and R2-mAb significantly worsened the Gal-N+LPS-induced cytotoxicity and apoptosis of SEC mediated by caspase-3, which were almost of similar magnitude to those in the in-vivo study. Galactosamine 76-81 ribonucleotide reductase M2 Mus musculus 42-44 17848680-1 2007 PURPOSE: To prospectively determine the cellular iron uptake by using R2 and R2* mapping with multiecho readout gradient-echo and spin-echo sequences. Iron 49-53 ribonucleotide reductase M2 Mus musculus 70-79 18500819-3 2008 The second RRM (RRM2) is necessary and sufficient for tight, sequence-specific binding to the uridine-rich sequences buried around the 5" splice sites. Uridine 94-101 ribonucleotide reductase M2 Mus musculus 11-14 18500819-3 2008 The second RRM (RRM2) is necessary and sufficient for tight, sequence-specific binding to the uridine-rich sequences buried around the 5" splice sites. Uridine 94-101 ribonucleotide reductase M2 Mus musculus 16-20 18500819-7 2008 Interestingly, this characteristic beta-loop structure is conserved among a number of RRMs, including the U2AF65 RRM2 and the Sex-lethal RRM1 and RRM2, which also bind to uridine-rich RNAs. Uridine 171-178 ribonucleotide reductase M2 Mus musculus 113-117 18500819-7 2008 Interestingly, this characteristic beta-loop structure is conserved among a number of RRMs, including the U2AF65 RRM2 and the Sex-lethal RRM1 and RRM2, which also bind to uridine-rich RNAs. Uridine 171-178 ribonucleotide reductase M2 Mus musculus 146-150 17848680-9 2007 R2 and R2* values were linearly correlated with cellular iron load, number of iron-loaded cells, and content of freely dissolved iron (r(2) range, 0.92-0.99; P < .001). Iron 57-61 ribonucleotide reductase M2 Mus musculus 0-9 17848680-9 2007 R2 and R2* values were linearly correlated with cellular iron load, number of iron-loaded cells, and content of freely dissolved iron (r(2) range, 0.92-0.99; P < .001). Iron 78-82 ribonucleotide reductase M2 Mus musculus 0-9 17848680-9 2007 R2 and R2* values were linearly correlated with cellular iron load, number of iron-loaded cells, and content of freely dissolved iron (r(2) range, 0.92-0.99; P < .001). Iron 78-82 ribonucleotide reductase M2 Mus musculus 0-9 17848680-13 2007 CONCLUSION: Quantitative R2 and R2* mapping enables noninvasive estimations of cellular iron load and number of iron-labeled cells. Iron 88-92 ribonucleotide reductase M2 Mus musculus 25-34 17848680-13 2007 CONCLUSION: Quantitative R2 and R2* mapping enables noninvasive estimations of cellular iron load and number of iron-labeled cells. Iron 112-116 ribonucleotide reductase M2 Mus musculus 25-34 12578384-5 2003 Analysis of the a-site D57N variant of mR1, which differs from wild-type mR1 (wt-mR1) in that its RR activity is activated by both ATP and dATP, demonstrates that dATP activation of the D57N variant RR arises from a blockage in the formation of mR1(4b) from mR1(4a), and provides strong evidence that mR1(4a) forms active complexes with mR2(2). 2'-deoxyadenosine triphosphate 163-167 ribonucleotide reductase M2 Mus musculus 337-340 16054677-2 2005 In common with other class Ia RRs, the enzyme is composed of two subunits (mR1 and mR2), with mR1 containing both the active site and allosteric effector sites and mR2 containing a stable tyrosyl radical that is essential for enzymatic activity. Tyrosyl radical 188-203 ribonucleotide reductase M2 Mus musculus 83-86 16054677-2 2005 In common with other class Ia RRs, the enzyme is composed of two subunits (mR1 and mR2), with mR1 containing both the active site and allosteric effector sites and mR2 containing a stable tyrosyl radical that is essential for enzymatic activity. Tyrosyl radical 188-203 ribonucleotide reductase M2 Mus musculus 164-167 15454215-2 2004 The enzyme is composed of two subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which disrupts mRR quaternary structure by competing with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 73-83 ribonucleotide reductase M2 Mus musculus 48-51 15454215-2 2004 The enzyme is composed of two subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which disrupts mRR quaternary structure by competing with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 73-83 ribonucleotide reductase M2 Mus musculus 133-136 15454215-2 2004 The enzyme is composed of two subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which disrupts mRR quaternary structure by competing with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 73-83 ribonucleotide reductase M2 Mus musculus 133-136 15586357-2 2005 The enzyme is composed of 2 subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which competes with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 71-81 ribonucleotide reductase M2 Mus musculus 46-49 15586357-2 2005 The enzyme is composed of 2 subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which competes with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 71-81 ribonucleotide reductase M2 Mus musculus 131-134 15586357-2 2005 The enzyme is composed of 2 subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which competes with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 71-81 ribonucleotide reductase M2 Mus musculus 131-134 35204799-0 2022 RRM2 Alleviates Doxorubicin-Induced Cardiotoxicity through the AKT/mTOR Signaling Pathway. Doxorubicin 16-27 ribonucleotide reductase M2 Mus musculus 0-4 12426144-8 2002 Fragment R1-2 was 90% homologous to a fragment of the DRIP/TRAP-80 (vitamin D receptor interacting protein/thyroid hormone receptor-activating protein 80) genes and was expressed in nontransformed but not in nickel-transformed cell lines. Nickel 208-214 ribonucleotide reductase M2 Mus musculus 9-13 9613846-7 1998 The lack of enzymatic activity in the mR1-cR2 complex is attributed to perturbation or elimination of interactions linking the tyrosine radical/dinuclear iron center and the C-terminus within R2. tyrosine radical 127-143 ribonucleotide reductase M2 Mus musculus 43-45 9613846-7 1998 The lack of enzymatic activity in the mR1-cR2 complex is attributed to perturbation or elimination of interactions linking the tyrosine radical/dinuclear iron center and the C-terminus within R2. Iron 154-158 ribonucleotide reductase M2 Mus musculus 43-45 34233591-5 2021 In an in vivo study, we established a streptozotocin-induced pregestational diabetes mellitus (PGDM) mouse model and found the fetal cardiac wall thickness in different regions to be dramatically increased in the PGDM grouValidation of DEMs and DEGs in the fetal heart showed significantly upregulated expression of let-7e-5p, miR-139-5p and miR-195-5p and downregulated expression of SGOL1, RRM2, RGS5, CDK1 and CENPA. Streptozocin 38-52 ribonucleotide reductase M2 Mus musculus 392-396 34249439-6 2021 Pterostilbene, a natural plant component, potently inhibited in vitro RR enzyme activity with the IC50 of about 0.62 muM through interacting with RRM2 protein, which was much higher than current RRM2 inhibitory drugs. pterostilbene 0-13 ribonucleotide reductase M2 Mus musculus 146-150 34249439-12 2021 This study demonstrates that pterostilbene is a novel potent RR inhibitor by targeting RRM2. pterostilbene 29-42 ribonucleotide reductase M2 Mus musculus 87-91 34207929-0 2021 Coumarin-Based Triapine Derivatives and Their Copper(II) Complexes: Synthesis, Cytotoxicity and mR2 RNR Inhibition Activity. 3-aminopyridine-2-carboxaldehyde thiosemicarbazone 15-23 ribonucleotide reductase M2 Mus musculus 96-99 34207929-5 2021 In addition, their ability to reduce the tyrosyl radical in mouse R2 protein of ribonucleotide reductase has been ascertained by EPR spectroscopy and the results were compared with those for triapine. cyclo(tyrosyl-tyrosyl) 41-48 ribonucleotide reductase M2 Mus musculus 66-68 34207929-5 2021 In addition, their ability to reduce the tyrosyl radical in mouse R2 protein of ribonucleotide reductase has been ascertained by EPR spectroscopy and the results were compared with those for triapine. 3-aminopyridine-2-carboxaldehyde thiosemicarbazone 191-199 ribonucleotide reductase M2 Mus musculus 66-68 12578384-1 2003 Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors. N,N-di-n-propylserotonin 13-17 ribonucleotide reductase M2 Mus musculus 113-116 12578384-1 2003 Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors. Free Radicals 88-100 ribonucleotide reductase M2 Mus musculus 113-116 12578384-1 2003 Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors. [[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate 147-170 ribonucleotide reductase M2 Mus musculus 113-116 12130552-7 2002 In contrast, mutation of this tryptophan to alanine in mR2 decreased the rate of internalization and inhibited basal signaling activity. Tryptophan 30-40 ribonucleotide reductase M2 Mus musculus 55-58 12130552-7 2002 In contrast, mutation of this tryptophan to alanine in mR2 decreased the rate of internalization and inhibited basal signaling activity. Alanine 44-51 ribonucleotide reductase M2 Mus musculus 55-58 11781084-2 2002 Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors. N,N-di-n-propylserotonin 13-17 ribonucleotide reductase M2 Mus musculus 113-116 11781084-2 2002 Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors. Free Radicals 88-100 ribonucleotide reductase M2 Mus musculus 113-116 11781084-2 2002 Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors. [[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate 147-170 ribonucleotide reductase M2 Mus musculus 113-116 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. Adenosine Triphosphate 115-118 ribonucleotide reductase M2 Mus musculus 102-104 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. Adenosine Triphosphate 115-118 ribonucleotide reductase M2 Mus musculus 319-321 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. 2'-deoxyadenosine triphosphate 122-126 ribonucleotide reductase M2 Mus musculus 102-104 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. 2'-deoxyadenosine triphosphate 122-126 ribonucleotide reductase M2 Mus musculus 319-321 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. Adenine 142-149 ribonucleotide reductase M2 Mus musculus 102-104 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. Adenine 142-149 ribonucleotide reductase M2 Mus musculus 319-321 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. Adenosine Triphosphate 123-126 ribonucleotide reductase M2 Mus musculus 102-104 11781084-4 2002 In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer. Adenosine Triphosphate 123-126 ribonucleotide reductase M2 Mus musculus 319-321 11781084-9 2002 Our results suggest that the R1(6)R2(6) heterohexamer is the major active form of the enzyme in mammalian cells, and that the ATP concentration is the primary modulator of enzyme activity, coupling the rate of DNA biosynthesis with the energetic state of the cell. Adenosine Triphosphate 126-129 ribonucleotide reductase M2 Mus musculus 34-36 11141086-1 2001 Mammalian ribonucleotide reductase, a chemotherapeutic target, has two subunits, mR1 and mR2, and is inhibited by AcF(1)TLDADF(7), denoted P7. tldadf 120-126 ribonucleotide reductase M2 Mus musculus 89-92 11015199-3 2000 Peptide 3 is a cyclic analogue of the N-acetylated form of the heptapeptide C-terminus of the mR2 subunit (Ac-FTLDADF), which is the link between the two subunits and previously shown to be the minimal sequence inhibitor mRR by competing with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 107-117 ribonucleotide reductase M2 Mus musculus 94-97 11015199-3 2000 Peptide 3 is a cyclic analogue of the N-acetylated form of the heptapeptide C-terminus of the mR2 subunit (Ac-FTLDADF), which is the link between the two subunits and previously shown to be the minimal sequence inhibitor mRR by competing with mR2 for binding to mR1. acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine 107-117 ribonucleotide reductase M2 Mus musculus 243-246 8783260-11 1996 In the molecular layer cells were found expressing N-methyl-D-aspartate R1-4 and N-methyl-D-aspartate R2B and cells in the granule layer were found to express N-methyl-D-aspartate R1-1, N-methyl-D-aspartate R1-3 and N-methyl-D-aspartate R1-4 and N-methyl-D-aspartate R2C only. N-Methylaspartate 51-71 ribonucleotide reductase M2 Mus musculus 72-76 34279079-0 2021 Triapine Analogues and Their Copper(II) Complexes: Synthesis, Characterization, Solution Speciation, Redox Activity, Cytotoxicity, and mR2 RNR Inhibition. 3-aminopyridine-2-carboxaldehyde thiosemicarbazone 0-8 ribonucleotide reductase M2 Mus musculus 135-138 34279079-11 2021 HL1 and 1 in the presence of 1,4-dithiothreitol are as potent inhibitors of mR2 ribonucleotide reductase as triapine. Dithiothreitol 29-47 ribonucleotide reductase M2 Mus musculus 76-79 34279079-11 2021 HL1 and 1 in the presence of 1,4-dithiothreitol are as potent inhibitors of mR2 ribonucleotide reductase as triapine. 3-aminopyridine-2-carboxaldehyde thiosemicarbazone 108-116 ribonucleotide reductase M2 Mus musculus 76-79 34234118-6 2021 Notably, knockdown of MYBL2 sensitized CRC cells to treatment with MK-1775, a clinical trial drug for inhibition of WEE1, which is involved in a degradation pathway of RRM2. adavosertib 67-74 ribonucleotide reductase M2 Mus musculus 168-172 35204799-4 2022 However, the specific function of RRM2 in DOX-induced cardiotoxicity is yet to be determined. Doxorubicin 42-45 ribonucleotide reductase M2 Mus musculus 34-38 35204799-5 2022 This study aimed to elucidate the role and potential mechanism of RRM2 on DOX-induced cardiotoxicity by investigating neonatal primary cardiomyocytes and mice treated with DOX. Doxorubicin 74-77 ribonucleotide reductase M2 Mus musculus 66-70 35204799-9 2022 RRM2 overexpression, on the contrary, alleviated DOX-induced cardiotoxicity in vivo and in vitro. Doxorubicin 49-52 ribonucleotide reductase M2 Mus musculus 0-4 35204799-10 2022 Consistently, DIDOX, an inhibitor of RRM2, attenuated the protective effect of RRM2. 3,4-dihydroxybenzohydroxamic acid 14-19 ribonucleotide reductase M2 Mus musculus 37-41 35204799-10 2022 Consistently, DIDOX, an inhibitor of RRM2, attenuated the protective effect of RRM2. 3,4-dihydroxybenzohydroxamic acid 14-19 ribonucleotide reductase M2 Mus musculus 79-83 35204799-11 2022 Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway. Doxorubicin 104-107 ribonucleotide reductase M2 Mus musculus 81-85 35204799-11 2022 Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway. Doxorubicin 104-107 ribonucleotide reductase M2 Mus musculus 158-162 35204799-11 2022 Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway. Doxorubicin 184-187 ribonucleotide reductase M2 Mus musculus 81-85 35204799-11 2022 Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway. Doxorubicin 184-187 ribonucleotide reductase M2 Mus musculus 158-162 35204799-12 2022 In conclusion, our experiment established that RRM2 could be a potential treatment in reversing DOX-induced cardiac dysfunction. Doxorubicin 96-99 ribonucleotide reductase M2 Mus musculus 47-51